title: Hemoglobin-ligand binding: understanding Hb function and allostery on atomic level.
abstract: The major physiological function of hemoglobin (Hb) is to bind oxygen in the lungs and deliver it to the tissues. This function is regulated and/or made efficient by endogenous heterotropic effectors. A number of synthetic molecules also bind to Hb to alter its allosteric activity. Our purpose is to review the current state of Hb structure and function that involves ensemble of tense and relaxed hemoglobin states and the dynamic equilibrium of the multistate due to the binding of endogenous heterotropic or synthetic allosteric effectors. The review also discusses the atomic interactions of synthetic ligands with the function or altered allosteric function of Hb that could be potentially harnessed for the treatment of diseases. This article is part of a Special Issue entitled: Protein Structure and Function in the Crystalline State.
authors.affiliation: Department of Medicinal Chemistry, School of Pharmacy and Institute for Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, VA 23219, USA. msafo@vcu.edu
authors.forename: Martin K
authors.initials: MK
authors.lastname: Safo
authors.forename: Mostafa H
authors.initials: MH
authors.lastname: Ahmed
authors.forename: Mohini S
authors.initials: MS
authors.lastname: Ghatge
authors.forename: Telih
authors.initials: T
authors.lastname: Boyiri
mesh_terms: D000495:Allosteric Site; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D006454:Hemoglobins; D008024:Ligands; D010100:Oxygen